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Volumn 42, Issue 1, 2009, Pages 75-83

Gene cloning, expression, and characterization of the geobacillus thermoleovorans CCR11 thermoalkaliphilic lipase

Author keywords

Gene cloning; Geobacillus thermoleovorans; Lipase; Thermophilic

Indexed keywords

CLONING VECTORS; E. COLI; EXPRESSION SYSTEM; FUSION TAG; GENE CLONING; GEOBACILLUS THERMOLEOVORANS; HIGH CONCENTRATION; LIPASE GENE; LIPOLYTIC ACTIVITY; OPEN READING FRAME; OPTIMAL ACTIVITY; PARENTAL STRAINS; SIGNAL PEPTIDE; STRUCTURAL GENE; SUBSTRATE SPECIFICITY; THERMOPHILIC;

EID: 69149097372     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12033-008-9136-6     Document Type: Article
Times cited : (28)

References (34)
  • 1
    • 0036669425 scopus 로고    scopus 로고
    • Lipases for biotechnology
    • DOI 10.1016/S0958-1669(02)00341-5
    • K-E Jaeger T Eggert 2002 Lipases for biotechnology Current Opinion in Biotechnology 13 390 397 10.1016/S0958-1669(02)00341-5 10.1016/S0958-1669(02) 00341-5 1:CAS:528:DC%2BD38XmsFOnsb8%3D (Pubitemid 35254099)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 390-397
    • Jaeger, K.-E.1    Eggert, T.2
  • 2
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: An overview of production, purification and biochemical properties
    • DOI 10.1007/s00253-004-1568-8
    • R Gupta N Gupta P Rathi 2004 Bacterial lipases: An overview of production, purification and biochemical properties Applied Microbiology and Biotechnology 64 763 781 10.1007/s00253-004-1568-8 10.1007/s00253-004-1568-8 1:CAS:528:DC%2BD2cXktlyku7Y%3D (Pubitemid 38918139)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.6 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 3
    • 84982614009 scopus 로고
    • Bacterial lipases
    • 10.1111/j.1574-6976.1994.tb00121.x 10.1111/j.1574-6976.1994.tb00121.x 1:CAS:528:DyaK2cXmsV2js7s%3D
    • K-E Jaeger S Ransac B Dijkstra C Colson M Heuvel O Misset 1994 Bacterial lipases FEMS Microbiology Reviews 15 29 63 10.1111/j.1574-6976.1994.tb00121.x 10.1111/j.1574-6976.1994.tb00121.x 1:CAS:528:DyaK2cXmsV2js7s%3D
    • (1994) FEMS Microbiology Reviews , vol.15 , pp. 29-63
    • Jaeger, K.-E.1    Ransac, S.2    Dijkstra, B.3    Colson, C.4    Heuvel, M.5    Misset, O.6
  • 4
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterization, and applications of lipases
    • DOI 10.1016/S0734-9750(01)00086-6, PII S0734975001000866
    • R Sharman C Yusuf U-C Banerjee 2001 Production, purification, characterization, and application of lipases Biotechnology Advances 19 627 662 10.1016/S0734-9750(01)00086-6 10.1016/S0734-9750(01)00086-6 (Pubitemid 34212866)
    • (2001) Biotechnology Advances , vol.19 , Issue.8 , pp. 627-662
    • Sharma, R.1    Chisti, Y.2    Banerjee, U.C.3
  • 5
    • 0037325495 scopus 로고    scopus 로고
    • Lipase assays for conventional and molecular screening: An overview
    • DOI 10.1042/BA20020059
    • R Gupta P Rathi N Gupta S Bradoo 2003 Lipase assay for conventional and molecular screening: an overview Biotechnology and Applied Biochemistry 37 63 71 10.1042/BA20020059 10.1042/BA20020059 1:CAS:528:DC%2BD3sXhtVOltr0%3D (Pubitemid 36246347)
    • (2003) Biotechnology and Applied Biochemistry , vol.37 , Issue.1 , pp. 63-71
    • Gupta, R.1    Rathi, P.2    Gupta, N.3    Bradoo, S.4
  • 6
    • 0037590011 scopus 로고    scopus 로고
    • Extremophiles as a source for novel enzymes
    • DOI 10.1016/S1369-5274(03)00060-2
    • B Van den Burg 2003 Extremophiles as a source for novel enzymes Current Opinion in Microbiology 6 213 218 10.1016/S1369-5274(03)00060-2 10.1016/S1369-5274(03)00060-2 (Pubitemid 36841663)
    • (2003) Current Opinion in Microbiology , vol.6 , Issue.3 , pp. 213-218
    • Van Den Burg, B.1
  • 7
    • 0035046039 scopus 로고    scopus 로고
    • Monoacylglycerol lipase from moderately thermophilic Bacillus sp. strain H-257: Molecular cloning, sequencing and expression in Escherichia coli of the gene
    • 1:CAS:528:DC%2BD3MXjtlSju7s%3D
    • S Kitaura K Suzuki S Imamura 2001 Monoacylglycerol lipase from moderately thermophilic Bacillus sp. strain H-257: molecular cloning, sequencing and expression in Escherichia coli of the gene Journal of Biochemistry 129 397 402 1:CAS:528:DC%2BD3MXjtlSju7s%3D
    • (2001) Journal of Biochemistry , vol.129 , pp. 397-402
    • Kitaura, S.1    Suzuki, K.2    Imamura, S.3
  • 8
    • 0141762453 scopus 로고    scopus 로고
    • Isolation and characterization of Bacillus sp. BP-6 LipA, a ubiquitous lipase among mesophilic Bacillus species
    • DOI 10.1046/j.1472-765X.2003.01413.x
    • C Ruiz J Pastor P Diaz 2003 Isolation and characterization of Bacillus sp. BP-6 LipA, a ubiquitous lipase among mesophilic Bacillus species Letters in Applied Microbiology 37 354 359 10.1046/j.1472-765X.2003.01413.x 10.1046/j.1472-765X.2003.01413.x 1:CAS:528:DC%2BD3sXovV2hur8%3D (Pubitemid 37186632)
    • (2003) Letters in Applied Microbiology , vol.37 , Issue.4 , pp. 354-359
    • Ruiz, C.1    Pastor, F.I.J.2    Diaz, P.3
  • 9
    • 37049017149 scopus 로고    scopus 로고
    • Identification and over-expression of a thermostable lipase from Geobacillus thermoleovorans Toshki in Escherichia coli
    • DOI 10.1016/j.micres.2006.02.004, PII S0944501306000218
    • Y Abdel-Fattah A Gaballa 2008 Identification and over-expression of a thermostable lipase from Geobacillus thermoleovorans Toshki in Escherichia coli Microbiological Research 163 13 20 10.1016/j.micres.2006.02.004 10.1016/j.micres.2006.02.004 1:CAS:528:DC%2BD1cXivVSjtLk%3D (Pubitemid 350251173)
    • (2008) Microbiological Research , vol.163 , Issue.1 , pp. 13-20
    • Abdel-Fattah, Y.R.1    Gaballa, A.A.2
  • 10
    • 0033966760 scopus 로고    scopus 로고
    • Expression of the Staphylococcus hyicus lipase in Lactococcus lactis
    • DOI 10.1128/AEM.66.2.588-598.2000
    • S Drouault G Corthier S Ehrlich P Renault 2000 Expression of Staphylococcus hyicus lipase in Lactococcus lactis Applied and Environmental Microbiology 66 588 598 10.1128/AEM.66.2.588-598.2000 10.1128/AEM.66.2.588-598. 2000 1:CAS:528:DC%2BD3cXhtFeru7s%3D (Pubitemid 30082745)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.2 , pp. 588-598
    • Drouault, S.1    Corthier, G.2    Ehrlich, S.D.3    Renault, P.4
  • 12
    • 0037358780 scopus 로고    scopus 로고
    • High-level expression of a lipase from Bacillus thermocatenulatus BTL2 in Pichia pastoris and some properties of the recombinant lipase
    • DOI 10.1016/S1046-5928(02)00679-4
    • D Quyen C Schmidt-Dannert R Schmid 2003 High-level expression of a lipase from Bacillus thermocatenulatus BTL2 in Pichia pastoris and some properties of the recombinant lipase Protein Expression and Purification 28 102 110 10.1016/S1046-5928(02)00679-4 10.1016/S1046-5928(02)00679-4 1:CAS:528: DC%2BD3sXitVKms78%3D (Pubitemid 36453184)
    • (2003) Protein Expression and Purification , vol.28 , Issue.1 , pp. 102-110
    • Quyen, D.T.1    Schmidt-Dannert, C.2    Schmid, R.D.3
  • 13
    • 0034134257 scopus 로고    scopus 로고
    • Thermostable lipase of Bacillus stearothermophilus: High-level production, purification, and calcium-dependent thermostability
    • 10.1271/bbb.64.280 10.1271/bbb.64.280 1:CAS:528:DC%2BD3cXhvVCjtro%3D
    • M-H Kim H-K Kim J-K Lee S-Y Park T-K Oh 2000 Thermostable lipase of Bacillus stearothermophilus: high-level production, purification, and calcium-dependent thermostability Bioscience, Biotechnology, and Biochemistry 64 280 286 10.1271/bbb.64.280 10.1271/bbb.64.280 1:CAS:528:DC%2BD3cXhvVCjtro%3D
    • (2000) Bioscience, Biotechnology, and Biochemistry , vol.64 , pp. 280-286
    • Kim, M.-H.1    Kim, H.-K.2    Lee, J.-K.3    Park, S.-Y.4    Oh, T.-K.5
  • 14
    • 0033451426 scopus 로고    scopus 로고
    • Rapid cloning of thermoalkalophilic lipases from Bacillus spp. using PCR
    • DOI 10.1023/A:1005654701905
    • P Bell H Nevalainen HW Morgan PL Bergquist 1999 Rapid cloning of thermoalkalophilic lipases from Bacillus spp. using PCR Biotechnology Letters 21 1003 1006 10.1023/A:1005654701905 10.1023/A:1005654701905 1:CAS:528: DyaK1MXotFSitb0%3D (Pubitemid 30041000)
    • (1999) Biotechnology Letters , vol.21 , Issue.11 , pp. 1003-1006
    • Bell, P.J.L.1    Nevalainen, H.2    Morgan, H.W.3    Bergquist, P.L.4
  • 15
    • 0034864538 scopus 로고    scopus 로고
    • Optimization of a thermostable lipase from Bacillus stearothermophilus p1: Overexpression, purification, and characterization
    • DOI 10.1006/prep.2001.1456
    • S Sinchaikul B Sookkheo S Phutrakul F-M Pan S-T Chen 2001 Optimization of a thermostable lipase from Bacillus stearothermophilus P1: overexpression, purification, and characterization Protein Expression and Purification 22 388 398 10.1006/prep.2001.1456 10.1006/prep.2001.1456 1:CAS:528:DC%2BD3MXlsFynt7g%3D (Pubitemid 32747915)
    • (2001) Protein Expression and Purification , vol.22 , Issue.3 , pp. 388-398
    • Sinchaikul, S.1    Sookkheo, B.2    Phutrakul, S.3    Pan, F.-M.4    Chen, S.-T.5
  • 16
    • 24944592023 scopus 로고    scopus 로고
    • Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11
    • DOI 10.1016/j.enzmictec.2005.06.003, PII S0141022905002292
    • LD Castro-Ochoa C Rodríguez-Gómez G Valerio-Alfaro RR Oliart 2005 Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11 Enzyme and Microbial Technology 37 648 654 10.1016/j.enzmictec.2005.06.003 10.1016/j.enzmictec.2005.06.003 1:CAS:528:DC%2BD2MXhtVWgsLrJ (Pubitemid 41306252)
    • (2005) Enzyme and Microbial Technology , vol.37 , Issue.6 , pp. 648-654
    • Castro-Ochoa, L.D.1    Rodriguez-Gomez, C.2    Valerio-Alfaro, G.3    Oliart Ros, R.4
  • 17
    • 70350617993 scopus 로고    scopus 로고
    • Short protocols in molecular biology. A compendium of methods from current protocols in molecular biology
    • Ausubel F., Brent R. R., Kingstone M. D., Seidman S. J., Struhl K. (Eds.) New York: Wiley
    • Ausubel, F., Brent, R. R., Kingstone, M. D., Seidman, S. J., & Struhl, K. (Eds.). (1997). Short protocols in molecular biology. A compendium of methods from current protocols in molecular biology, vol 1 Preparation and analysis of DNA and Enzymatic manipulation of DNA (pp. 2-1-3-50). New York: Wiley.
    • (1997) Preparation and Analysis of DNA and Enzymatic Manipulation of DNA , vol.1 , pp. 21-350
  • 18
    • 0023089142 scopus 로고
    • Specific and sensitive plate assay for bacterial lipases
    • 1:CAS:528:DyaL2sXotFehtQ%3D%3D
    • G Kouker K Jaeger 1987 Specific and sensitive plate assay for bacterial lipases Applied and Environmental Microbiology 53 211 213 1:CAS:528: DyaL2sXotFehtQ%3D%3D
    • (1987) Applied and Environmental Microbiology , vol.53 , pp. 211-213
    • Kouker, G.1    Jaeger, K.2
  • 19
    • 0031722751 scopus 로고    scopus 로고
    • A novel thermostable lipase from a thermophilic Bacillus sp.: Characterization and esterification studies
    • 10.1023/A:1005430215849 10.1023/A:1005430215849 1:CAS:528: DyaK1cXotFCntbw%3D
    • N Nawani N Dosanjh J Kaur 1998 A novel thermostable lipase from a thermophilic Bacillus sp.: characterization and esterification studies Biotechnology Letters 20 997 1000 10.1023/A:1005430215849 10.1023/A: 1005430215849 1:CAS:528:DyaK1cXotFCntbw%3D
    • (1998) Biotechnology Letters , vol.20 , pp. 997-1000
    • Nawani, N.1    Dosanjh, N.2    Kaur, J.3
  • 20
    • 0019551730 scopus 로고
    • "western Blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • 10.1016/0003-2697(81)90281-5 10.1016/0003-2697(81)90281-5 1:CAS:528:DyaL3MXhvVOqtbs%3D
    • W Burnette 1981 "Western Blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A Analytical Biochemistry 112 195 203 10.1016/0003-2697(81)90281-5 10.1016/0003-2697(81)90281-5 1:CAS:528:DyaL3MXhvVOqtbs%3D
    • (1981) Analytical Biochemistry , vol.112 , pp. 195-203
    • Burnette, W.1
  • 22
    • 0038353703 scopus 로고    scopus 로고
    • Use of methylumbeliferyl-derivative substrates for lipase activity characterization
    • DOI 10.1016/S1381-1177(03)00048-1
    • N Prim M Sánchez C Ruiz J Pastor P Diaz 2003 Use of methylumbeliferyl-derivative substrate for lipase activity characterization Journal of Molecular Catalysis B, Enzymatic 22 339 346 10.1016/S1381-1177(03) 00048-1 10.1016/S1381-1177(03)00048-1 1:CAS:528:DC%2BD3sXltVSktL4%3D (Pubitemid 36802034)
    • (2003) Journal of Molecular Catalysis B: Enzymatic , vol.22 , Issue.5-6 , pp. 339-346
    • Prim, N.1    Sanchez, M.2    Ruiz, C.3    Pastor, F.I.J.4    Diaz, P.5
  • 23
    • 0029899631 scopus 로고    scopus 로고
    • Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. Molecular cloning, nucleotide sequence, purification and some properties
    • C Schmidt-Dannert L Rúa H Atomi R Schnmid 1996 Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. Molecular cloning, nucleotide sequence, purification and some properties Biochimica et Biophysica Acta 1301 105 114
    • (1996) Biochimica et Biophysica Acta , vol.1301 , pp. 105-114
    • Schmidt-Dannert, C.1    Rúa, L.2    Atomi, H.3    Schnmid, R.4
  • 24
    • 4544341220 scopus 로고    scopus 로고
    • High level expression of thermostable lipase from Geobacillus sp. strain T1
    • DOI 10.1271/bbb.68.96
    • T Leow R Rahman M Basri A Salleh 2004 High level expression of thermostable lipase from Geobacillus sp strain T1 Bioscience, Biotechnology, and Biochemistry 68 96 103 10.1271/bbb.68.96 10.1271/bbb.68.96 1:CAS:528: DC%2BD2cXhtFKgtro%3D (Pubitemid 39251570)
    • (2004) Bioscience, Biotechnology and Biochemistry , vol.68 , Issue.1 , pp. 96-103
    • Leow, T.C.1    Rahman, R.N.Z.R.A.2    Basri, M.3    Salleh, A.B.4
  • 25
    • 17844392864 scopus 로고    scopus 로고
    • Combining prediction of secondary structure and solvent accessibility in proteins
    • DOI 10.1002/prot.20441
    • A Adamczak JM Porollo 2005 Combining prediction of secondary structure and solvent accessibility in proteins Proteins: Structure, Function, and Bioinformatics 59 467 475 10.1002/prot.20441 10.1002/prot.20441 (Pubitemid 40594291)
    • (2005) Proteins: Structure, Function and Genetics , vol.59 , Issue.3 , pp. 467-475
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 26
    • 0037604815 scopus 로고    scopus 로고
    • Cloning and expression of a novel lipase gene from Bacillus sphaericus 205y
    • 1:CAS:528:DC%2BD3sXjvVagtbY%3D
    • R Rahman J Chin A Salleh 2003 Cloning and expression of a novel lipase gene from Bacillus sphaericus 205y Molecular Genetics and Genomics 269 252 260 1:CAS:528:DC%2BD3sXjvVagtbY%3D
    • (2003) Molecular Genetics and Genomics , vol.269 , pp. 252-260
    • Rahman, R.1    Chin, J.2    Salleh, A.3
  • 27
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • DOI 10.1042/0264-6021:3430177
    • J Arpigny K-L Jaeger 1999 Bacterial lipolytic enzymes: Classification and properties The Biochemical Journal 343 177 183 10.1042/0264-6021:3430177 10.1042/0264-6021:3430177 1:CAS:528:DyaK1MXmvVyju7o%3D (Pubitemid 29473893)
    • (1999) Biochemical Journal , vol.343 , Issue.1 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.-E.2
  • 28
    • 0036431593 scopus 로고    scopus 로고
    • Crystal structure of a thermostable lipase from Bacillus stearothermophilus P1
    • DOI 10.1016/S0022-2836(02)01004-5
    • J Tyndall S Sinchaikul T Fothergill-Gilmore M Walkinshaw 2002 Crystal structure of a thermostable lipase from Bacillus stearothermophilus P1 Journal of Molecular Biology 323 859 869 10.1016/S0022-2836(02)01004-5 10.1016/S0022-2836(02)01004-5 1:CAS:528:DC%2BD38Xot1Knu7c%3D (Pubitemid 35341060)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.5 , pp. 859-869
    • Tyndall, J.D.A.1    Sinchaikul, S.2    Fothergill-Gilmore, L.A.3    Taylor, P.4    Walkinshaw, M.D.5
  • 29
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • DOI 10.1146/annurev.micro.53.1.315
    • K-E Jaeger B Dijkstra M Reetz 1999 Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases Annual Review of Microbiology 53 315 351 10.1146/annurev.micro.53.1.315 10.1146/annurev.micro.53.1.315 1:CAS:528:DyaK1MXmvVOnsb4%3D (Pubitemid 29503734)
    • (1999) Annual Review of Microbiology , vol.53 , pp. 315-351
    • Jaeger, K.-E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 30
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • DOI 10.1128/MMBR.65.1.1-43.2001
    • C Vieille G Zeikus 2001 Hyperthermopilic enzymes: source, uses, and molecular mechanism for thermostability Microbiology and Molecular Biology Reviews 65 1 43 10.1128/MMBR.65.1.1-43.2001 10.1128/MMBR.65.1.1-43.2001 1:CAS:528:DC%2BD3MXisFyms74%3D (Pubitemid 32204286)
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 31
    • 4143110558 scopus 로고    scopus 로고
    • Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase
    • DOI 10.1016/j.jmb.2004.06.059, PII S0022283604007636
    • P Acharya E Rajakumara R Sankaranarayanana N Rao 2004 Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase Journal of Molecular Biology 341 1271 1281 10.1016/j.jmb.2004.06.059 10.1016/j.jmb.2004.06.059 1:CAS:528:DC%2BD2cXmsVCrtLk%3D (Pubitemid 39092314)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1271-1281
    • Acharya, P.1    Rajakumara, E.2    Sankaranarayanan, R.3    Rao, N.M.4
  • 33
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • DOI 10.1006/jmbi.1997.1042
    • G Vogt S Woell P Argos 1997 Protein thermal stability, hydrogen bonds, and ion pairs Journal of Molecular Biology 269 631 643 10.1006/jmbi.1997.1042 10.1006/jmbi.1997.1042 1:CAS:528:DyaK2sXktlejtbw%3D (Pubitemid 27267875)
    • (1997) Journal of Molecular Biology , vol.269 , Issue.4 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 34
    • 0034684070 scopus 로고    scopus 로고
    • Influence of lid conformation on lipase enantioselectivity
    • DOI 10.1016/S1381-1177(99)00110-1, PII S1381117799001101
    • P Overbeeke C Govardhan N Khalaf J Jongejan J Heijnen 2000 Influence of lid conformation on lipase enantioselectivity Journal of Molecular Catalysis B, Enzymatic 10 385 393 10.1016/S1381-1177(99)00110-1 10.1016/S1381-1177(99)00110-1 1:CAS:528:DC%2BD3cXltlWgtr8%3D (Pubitemid 30483992)
    • (2000) Journal of Molecular Catalysis - B Enzymatic , vol.10 , Issue.4 , pp. 385-393
    • Overbeeke, P.L.A.1    Govardhan, C.2    Khalaf, N.3    Jongejan, J.A.4    Heijnen, J.J.5


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